Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F11%3A00360786" target="_blank" >RIV/61388971:_____/11:00360786 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.molcatb.2011.03.008" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2011.03.008</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.molcatb.2011.03.008" target="_blank" >10.1016/j.molcatb.2011.03.008</a>
Alternative languages
Result language
angličtina
Original language name
Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction
Original language description
The transformation of benzonitrile into benzohydroxamic acid was performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step was catalyzed by either a cell-free extract from Rhodococcus erythropolis A4 (nitrile hydratase) or cell-free extracts from recombinant Escherichia coli strains expressing nitrile hydratases from Raoultella terrigena 77.1 and Klebsiella oxytoca 38.1.2; the biocatalyst in the second stepwas a cellfree extract from R. erythropolis A4 (amidase). When using the cell-free extract from R. erythropolis A4 in the first step, the hydrolytic amidase activity was suppressed by ammonium ions, which, however, did not inhibit the acyl transfer reaction catalyzed by the same enzyme. Aromatic and aliphatic nitriles were examined as substrates of the recombinant nitrile hydratases by using a colorimetric assay of hydroxamic acids produced in a coupled acyl transfer reaction
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Catalysis B-Enzymatic
ISSN
1381-1177
e-ISSN
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Volume of the periodical
71
Issue of the periodical within the volume
1
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
5
Pages from-to
51-55
UT code for WoS article
000291451000008
EID of the result in the Scopus database
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